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| Melis Arslan; Markus J. Buehler. |
| Silk is an ancient but remarkably strong, extensible and tough material made from simple protein building blocks. Earlier work has shown that the particular molecular geometry of silk with a composite of semi-amorphous and nanocrystalline beta-sheet protein domains provides the structural basis for its characteristic softening-stiffening behavior and remarkable strength at the nanoscale. Yet, an open question remains as to how these nanoscale properties are upscaled so effectively to create strong, extensible and tough silk fibers. Here we discover that the geometric confinement of fibrils to ≈50-100 nm width and arranged in bundles to form larger-scale silk fibers, is the key to explaining the upscaling of the mechanical properties of silk from... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics; Earth & Environment. |
| Ano: 2011 |
URL: http://precedings.nature.com/documents/5916/version/1 |
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| Tristan Giesa; Melis Arslan; Nicola Pugno; Markus J. Buehler. |
| Silk is an exceptionally strong, extensible and tough material made from simple protein building blocks. The molecular structure of dragline spider silk repeat units consists of semi-amorphous and nanocrystalline beta-sheet protein domains. Here we show by a series of computational experiments how the nanoscale properties of silk repeat units are scaled up to create macroscopic silk fibers with outstanding mechanical properties despite the presence of cavities, tears and cracks. We demonstrate that the geometric confinement of silk fibrils to diameters of 50±30 nm width is critical to facilitate a powerful mechanism by which hundreds of thousands of protein domains synergistically resist deformation and failure to provide enhanced strength,... |
| Tipo: Manuscript |
Palavras-chave: Biotechnology; Chemistry; Bioinformatics; Earth & Environment. |
| Ano: 2011 |
URL: http://precedings.nature.com/documents/5916/version/2 |
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